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2CA0

Crystal structure of YC-17-bound cytochrome P450 PikC (CYP107L1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0017000biological_processantibiotic biosynthetic process
A0020037molecular_functionheme binding
A0033068biological_processmacrolide biosynthetic process
A0046872molecular_functionmetal ion binding
A0055114biological_processobsolete oxidation-reduction process
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0017000biological_processantibiotic biosynthetic process
B0020037molecular_functionheme binding
B0033068biological_processmacrolide biosynthetic process
B0046872molecular_functionmetal ion binding
B0055114biological_processobsolete oxidation-reduction process
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM A1407
ChainResidue
ALEU93
APRO289
ATHR294
AARG296
AALA346
APHE347
AGLY348
AILE351
AHIS352
APHE353
ACYS354
AHIS100
AALA360
AARG104
AILE239
ALEU240
AALA243
AGLY244
ATHR247
ATHR248

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PXI A1408
ChainResidue
AGLU85
ALEU88
AASN89
AGLU94
APHE178
AHIS238
AALA243
AGLU246
ATHR247
AVAL290
AASN392
AMET394
AILE395
AHOH2032

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM B1407
ChainResidue
BMET92
BLEU93
BHIS100
BARG104
BPHE111
BALA243
BGLY244
BTHR247
BTHR248
BALA293
BTHR294
BARG296
BALA346
BPHE347
BGLY348
BILE351
BHIS352
BCYS354
BPXI1408

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PXI B1408
ChainResidue
BTRP74
BGLU85
BLEU93
BGLU94
BPHE178
BHIS238
BVAL242
BALA243
BGLU246
BVAL290
BTHR294
BASN392
BILE395
BHEM1407

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGIHFCIG
ChainResidueDetails
APHE347-GLY356

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459
ChainResidueDetails
AGLU94
AALA187
AHIS238
BGLU94
BALA187
BHIS238

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459, ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965, ECO:0000312|PDB:2C6H, ECO:0000312|PDB:2C7X, ECO:0000312|PDB:2CA0, ECO:0000312|PDB:2CD8, ECO:0000312|PDB:2VZ7, ECO:0000312|PDB:2VZM, ECO:0000312|PDB:2WHW, ECO:0000312|PDB:2WI9, ECO:0000312|PDB:3ZK5, ECO:0000312|PDB:4B7D, ECO:0000312|PDB:4B7S, ECO:0000312|PDB:4BF4
ChainResidueDetails
ACYS354
BCYS354

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
AGLU246
ATHR247

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
BGLU246
BTHR247

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PDB entries from 2024-08-14

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